Evidence map›Paper›PMID 28336315›Full record

ReviewBiochimica et biophysica acta. Biomembranes2017

Cardiolipin and mitochondrial cristae organization.

Nikita Ikon, Robert O Ryan

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta. Biomembranes, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 198 papers.

0numbers the graph read from it
0cells of the map it votes in
198citing papers in PubMed
11.0field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

198 citing papers in PubMed, 327 citations in OpenAlex.

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138 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Nikita IkonChildren's Hospital Oakland Research Institute, 5700 Martin Luther King Jr. Way, Oakland, CA 94609, United States.
Robert O RyanChildren's Hospital Oakland Research Institute, 5700 Martin Luther King Jr. Way, Oakland, CA 94609, United States. Electronic address: rryan@chori.org.
Martin Luther King, Jr. Multi-Service Ambulatory Care Center · US

Funding

Effect of Apolipoprotein Structural AdaptabilityR37HL064159 · NHLBI · UNIVERSITY OF NEVADA RENO · PI RYAN, ROBERT O'MARA · 2010 to 2019
$4.1M
EFFECT OF APOLIPOPROTEIN STRUCTURAL ADAPTABILITYR01HL064159 · NHLBI · CHILDREN'S HOSPITAL &RES CTR AT OAKLAND · PI RYAN, ROBERT O'MARA · 2000 to 2009
$3.6M
Pre-doctoral Training in Molecular and Biochemical NutritionT32DK061918 · NIDDK · UNIVERSITY OF CALIFORNIA BERKELEY · PI NAPOLI, JOSEPH L · 2002 to 2016
$2.6M
NHLBI NIH HHS R01 HL064159NHLBI NIH HHS R37 HL064159NIDDK NIH HHS T32 DK061918
6 · The paper itself

Abstract

A fundamental question in cell biology, under investigation for over six decades, is the structural organization of mitochondrial cristae. Long known to harbor electron transport chain proteins, crista membrane integrity is key to establishment of the proton gradient that drives oxidative phosphorylation. Visualization of cristae morphology by electron microscopy/tomography has provided evidence that cristae are tube-like extensions of the mitochondrial inner membrane (IM) that project into the matrix space. Reconciling ultrastructural data with the lipid composition of the IM provides support for a continuously curved cylindrical bilayer capped by a dome-shaped tip. Strain imposed by the degree of curvature is relieved by an asymmetric distribution of phospholipids in monolayer leaflets that comprise cristae membranes. The signature mitochondrial lipid, cardiolipin (~18% of IM phospholipid mass), and phosphatidylethanolamine (34%) segregate to the negatively curved monolayer leaflet facing the crista lumen while the opposing, positively curved, matrix-facing monolayer leaflet contains predominantly phosphatidylcholine. Associated with cristae are numerous proteins that function in distinctive ways to establish and/or maintain their lipid repertoire and structural integrity. By combining unique lipid components with a set of protein modulators, crista membranes adopt and maintain their characteristic morphological and functional properties. Once established, cristae ultrastructure has a direct impact on oxidative phosphorylation, apoptosis, fusion/fission as well as diseases of compromised energy metabolism.

Indexed as

Oxidative PhosphorylationAcyltransferasesBlood ProteinsCardiolipinsGene Expression RegulationGTP PhosphohydrolasesHumansMembrane ProteinsMitochondriaMitochondrial DynamicsMitochondrial MembranesMitochondrial ProteinsPhosphatidylcholinesPhosphatidylethanolaminesProhibitinsRepressor ProteinsAcyltransferasesBlood ProteinsCardiolipinsGTP PhosphohydrolasesMembrane ProteinsMitochondrial ProteinsOPA1 protein, humanPhosphatidylcholinesphosphatidylethanolaminePhosphatidylethanolaminesProhibitinsRepressor ProteinsSTOML2 protein, humanTAFAZZIN protein, humanTranscription FactorsCardiolipinCristaeElectron transport chainMembrane curvatureMitochondriaNon-bilayer lipidPhospholipid

Identifiers

PMID28336315
PMCPMC5426559
OpenAlexW2601743360

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.